Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium

M. P. Kavanaugh; R. S. Hurst; J. Yakel; M. D. Varnum; J. P. Adelman; R. A. North

doi:10.1016/0896-6273(92)90277-K

Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium

M. P. Kavanaugh
, R. S. Hurst
, J. Yakel
, M. D. Varnum
, J. P. Adelman
, R. A. North

Oregon Health and Science University

Research output: Contribution to journal › Article › peer-review

127 Scopus citations

Abstract

RNAs encoding a wild-type (RBK1) and a mutant (RBK1(Y379V,V381 T); RBK1^*) subunit of voltage-dependent potassium channels were injected into Xenopus oocytes. When expressed separately, they made homotetrameric channels that differed about 100-fold in sensitivity to tetraethylammonium (TEA). Mixtures of channels having one, two, or three low affinity subunits were expressed by injecting various proportions of RBK1 and RBK1^* RNAs. The affinity for TEA of these three channel species was deduced by fitting concentration-response curves for the inhibition of potassium currents. DNAs were also concatenated to construct a sequence that encoded two connected subunits, and channels that contained four, two, or no TEA-sensitive subunits were expressed. The results suggest that bound TEA interacts simultaneously with all four subunits.

Original language	English
Pages (from-to)	493-497
Number of pages	5
Journal	Neuron
Volume	8
Issue number	3
DOIs	https://doi.org/10.1016/0896-6273(92)90277-K
State	Published - Mar 1992

Funding

We thank Yan-na Wu for expertly injecting oocytes. This work was supported by grants from the ADAMHA (DA03160) and from the National Institutes of Health (NS28504). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC Section 1734 solely to indicate this fact.

Funder number
DA03160
NS28504
R37DA003160

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10.1016/0896-6273(92)90277-K

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title = "Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium",

abstract = "RNAs encoding a wild-type (RBK1) and a mutant (RBK1(Y379V,V381 T); RBK1*) subunit of voltage-dependent potassium channels were injected into Xenopus oocytes. When expressed separately, they made homotetrameric channels that differed about 100-fold in sensitivity to tetraethylammonium (TEA). Mixtures of channels having one, two, or three low affinity subunits were expressed by injecting various proportions of RBK1 and RBK1* RNAs. The affinity for TEA of these three channel species was deduced by fitting concentration-response curves for the inhibition of potassium currents. DNAs were also concatenated to construct a sequence that encoded two connected subunits, and channels that contained four, two, or no TEA-sensitive subunits were expressed. The results suggest that bound TEA interacts simultaneously with all four subunits.",

author = "Kavanaugh, \{M. P.\} and Hurst, \{R. S.\} and J. Yakel and Varnum, \{M. D.\} and Adelman, \{J. P.\} and North, \{R. A.\}",

note = "Funding Information: We thank Yan-na Wu for expertly injecting oocytes. This work was supported by grants from the ADAMHA (DA03160) and from the National Institutes of Health (NS28504). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC Section 1734 solely to indicate this fact.",

year = "1992",

month = mar,

doi = "10.1016/0896-6273(92)90277-K",

language = "English",

volume = "8",

pages = "493--497",

journal = "Neuron",

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T1 - Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium

AU - Kavanaugh, M. P.

AU - Hurst, R. S.

AU - Yakel, J.

AU - Varnum, M. D.

AU - Adelman, J. P.

AU - North, R. A.

N1 - Funding Information: We thank Yan-na Wu for expertly injecting oocytes. This work was supported by grants from the ADAMHA (DA03160) and from the National Institutes of Health (NS28504). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC Section 1734 solely to indicate this fact.

PY - 1992/3

Y1 - 1992/3

N2 - RNAs encoding a wild-type (RBK1) and a mutant (RBK1(Y379V,V381 T); RBK1*) subunit of voltage-dependent potassium channels were injected into Xenopus oocytes. When expressed separately, they made homotetrameric channels that differed about 100-fold in sensitivity to tetraethylammonium (TEA). Mixtures of channels having one, two, or three low affinity subunits were expressed by injecting various proportions of RBK1 and RBK1* RNAs. The affinity for TEA of these three channel species was deduced by fitting concentration-response curves for the inhibition of potassium currents. DNAs were also concatenated to construct a sequence that encoded two connected subunits, and channels that contained four, two, or no TEA-sensitive subunits were expressed. The results suggest that bound TEA interacts simultaneously with all four subunits.

AB - RNAs encoding a wild-type (RBK1) and a mutant (RBK1(Y379V,V381 T); RBK1*) subunit of voltage-dependent potassium channels were injected into Xenopus oocytes. When expressed separately, they made homotetrameric channels that differed about 100-fold in sensitivity to tetraethylammonium (TEA). Mixtures of channels having one, two, or three low affinity subunits were expressed by injecting various proportions of RBK1 and RBK1* RNAs. The affinity for TEA of these three channel species was deduced by fitting concentration-response curves for the inhibition of potassium currents. DNAs were also concatenated to construct a sequence that encoded two connected subunits, and channels that contained four, two, or no TEA-sensitive subunits were expressed. The results suggest that bound TEA interacts simultaneously with all four subunits.

UR - https://www.scopus.com/pages/publications/0026533326

U2 - 10.1016/0896-6273(92)90277-K

DO - 10.1016/0896-6273(92)90277-K

M3 - Article

C2 - 1550674

AN - SCOPUS:0026533326

SN - 0896-6273

VL - 8

SP - 493

EP - 497

JO - Neuron

JF - Neuron

IS - 3

ER -

Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium

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